CNDD3_ARATH
ID CNDD3_ARATH Reviewed; 1314 AA.
AC O24610; O23639; Q7DLS9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Condensin-2 complex subunit CAP-D3 {ECO:0000303|PubMed:22855829, ECO:0000303|PubMed:23929493};
DE AltName: Full=Protein CHROMOSOME-ASSOCIATED POLYPEPTIDE D-3 {ECO:0000303|PubMed:23929493};
DE Short=AtCap-D3 {ECO:0000303|PubMed:23929493};
GN Name=CAP-D3 {ECO:0000303|PubMed:22855829, ECO:0000303|PubMed:23929493};
GN OrderedLocusNames=At4g15890 {ECO:0000312|Araport:AT4G15890};
GN ORFNames=Dl3985W {ECO:0000312|EMBL:CAB45995.1},
GN FCAALL.407 {ECO:0000312|EMBL:CAB78631.1},
GN G14587-6 {ECO:0000312|EMBL:CAA72072.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 628-1299.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=9358062; DOI=10.1016/s0378-1119(97)00374-0;
RA Aubourg S., Takvorian A., Cheron A., Kreis M., Lecharny A.;
RT "Structure, organization and putative function of the genes identified
RT within a 23.9 kb fragment from Arabidopsis thaliana chromosome IV sequenced
RT in the framework of the ESSA programme.";
RL Gene 199:241-253(1997).
RN [5]
RP REVIEW.
RX PubMed=22855829; DOI=10.1101/gad.194746.112;
RA Hirano T.;
RT "Condensins: universal organizers of chromosomes with diverse functions.";
RL Genes Dev. 26:1659-1678(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23929493; DOI=10.1007/s00412-013-0424-y;
RA Schubert V., Lermontova I., Schubert I.;
RT "The Arabidopsis CAP-D proteins are required for correct chromatin
RT organisation, growth and fertility.";
RL Chromosoma 122:517-533(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25065716; DOI=10.1111/tpj.12628;
RA Smith S.J., Osman K., Franklin F.C.;
RT "The condensin complexes play distinct roles to ensure normal chromosome
RT morphogenesis during meiotic division in Arabidopsis.";
RL Plant J. 80:255-268(2014).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY MMD1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27385818; DOI=10.1105/tpc.16.00040;
RA Wang J., Niu B., Huang J., Wang H., Yang X., Dong A., Makaroff C., Ma H.,
RA Wang Y.;
RT "The PHD Finger Protein MMD1/DUET Ensures the Progression of Male Meiotic
RT Chromosome Condensation and Directly Regulates the Expression of the
RT Condensin Gene CAP-D3.";
RL Plant Cell 28:1894-1909(2016).
CC -!- FUNCTION: Regulatory subunit of the condensin-2 complex, a complex
CC which establishes mitotic chromosome architecture and is involved in
CC physical rigidity of the chromatid axis (By similarity). May promote
CC the resolution of double-strand DNA catenanes (intertwines) between
CC sister chromatids (By similarity). Required for plant vigor, fertility,
CC chromatin condensation and sister chromatid cohesion both during
CC mitosis and meiosis (PubMed:23929493, PubMed:27385818). Necessary to
CC maintain normal structural integrity of the meiotic chromosomes during
CC the two nuclear divisions of gametogenesis, especially to prevent
CC interchromosome connections at metaphase I (PubMed:25065716). Seems
CC also involved in crossover formation during meiotic prophase I
CC (PubMed:25065716). Prevents centromeric and pericentromeric
CC heterochromatin repeats association (PubMed:23929493).
CC {ECO:0000250|UniProtKB:P42695, ECO:0000269|PubMed:23929493,
CC ECO:0000269|PubMed:25065716, ECO:0000269|PubMed:27385818}.
CC -!- SUBUNIT: Component of the condensin-2 complex.
CC {ECO:0000250|UniProtKB:P42695}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:27385818}. Chromosome
CC {ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716,
CC ECO:0000269|PubMed:27385818}. Note=Observed throughout euchromatic
CC nucleoplasm (PubMed:23929493, PubMed:27385818). Associates with the
CC chromosomes throughout meiosis (PubMed:25065716).
CC {ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716,
CC ECO:0000269|PubMed:27385818}.
CC -!- TISSUE SPECIFICITY: Present in buds. {ECO:0000269|PubMed:25065716}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed at bolting, flowering and during
CC seed formation. {ECO:0000269|PubMed:23929493}.
CC -!- INDUCTION: Regulated in a cell cycle-dependent manner with an increase
CC during G2 phase, highest levels in the middle of G2 and a drop during
CC mitosis (PubMed:23929493). Induced by MMD1 (PubMed:27385818).
CC {ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:27385818}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with small rosette leaves
CC (PubMed:25065716). Reduced pollen fertility and seed set
CC (PubMed:23929493, PubMed:27385818). Lower chromatin density and
CC frequent (peri)centromere association in interphase nuclei as well as
CC impaired sister chromatid cohesion (PubMed:23929493). Altered
CC interphase chromatin architecture in differentiated nuclei
CC (PubMed:23929493). Defect chromosome condensation in male meiocytes and
CC in centromeres orientation (PubMed:27385818). During meiosis, extensive
CC interchromosome connections at metaphase I as well as a slight
CC reduction in crossover formation (PubMed:25065716).
CC {ECO:0000269|PubMed:23929493, ECO:0000269|PubMed:25065716,
CC ECO:0000269|PubMed:27385818}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z97339; CAB45995.1; -; Genomic_DNA.
DR EMBL; AL161542; CAB78631.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83663.1; -; Genomic_DNA.
DR EMBL; Y11156; CAA72043.1; -; mRNA.
DR EMBL; Y11187; CAA72072.1; -; Genomic_DNA.
DR PIR; A85176; A85176.
DR PIR; F71424; F71424.
DR RefSeq; NP_193324.1; NM_117681.3.
DR AlphaFoldDB; O24610; -.
DR STRING; 3702.AT4G15890.1; -.
DR PaxDb; O24610; -.
DR PRIDE; O24610; -.
DR ProteomicsDB; 176936; -.
DR EnsemblPlants; AT4G15890.1; AT4G15890.1; AT4G15890.
DR GeneID; 827271; -.
DR Gramene; AT4G15890.1; AT4G15890.1; AT4G15890.
DR Araport; AT4G15890; -.
DR TAIR; locus:2130869; AT4G15890.
DR eggNOG; KOG0413; Eukaryota.
DR HOGENOM; CLU_002301_1_0_1; -.
DR InParanoid; O24610; -.
DR OMA; RIHPNIC; -.
DR OrthoDB; 60751at2759; -.
DR PhylomeDB; O24610; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O24610; baseline and differential.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IEA:InterPro.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0098653; P:centromere clustering; IMP:TAIR.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IMP:UniProtKB.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IEP:UniProtKB.
DR GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR012371; NCAPD3.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR Pfam; PF12717; Cnd1; 1.
DR PIRSF; PIRSF036508; Condns_HCP-6; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Chromosome; DNA condensation; Meiosis; Mitosis;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1314
FT /note="Condensin-2 complex subunit CAP-D3"
FT /id="PRO_0000454773"
FT REPEAT 20..58
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 98..136
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 184..222
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 231..267
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 269..310
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 331..360
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 361..398
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 417..455
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 457..493
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 494..532
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 821..859
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 878..916
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 917..954
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 956..992
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1053..1091
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1138..1179
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REGION 116..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 789..796
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1282..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1096
FT /note="I -> T (in Ref. 4; CAA72043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1314 AA; 144738 MW; CB23CD062CCE625A CRC64;
MDEELLLTRI LAGIEGGDDE SDYHELVTDL KSLLDTDDDE ILNRFYGSLS SMASSFLRCI
SAAMDSPVES GRLAILASDA YLSLLLSTNC PVFTFFSPIA FLSLLGSIRR YLKRRDDSAG
QGSNSQREKG NKKKRGRGKR NLGYEDGEET EEGGFDAKLM FIVLEKLGSV LSFVHLDRFP
DSLKSLVQTV SEIPLLALEH SGVLNYDRLM EMCGKILGGV LNSDHGDMAL TAAEISKSLT
PLLLMGKHQA RSFALGFVSR KLMSLAKDNP ELKKVVSNLP KFLVHKAPEK AEPRGFAVEA
VLEIVKAMEV EGQSEFVDFV MKMCQGKSNF RVLAVDIIPL LISSLGNPLG DISSENGLKD
SWGLGCIDAL VQRCSDTSAL IRARALSNLA QVVEFLSGDE RSRSILKQAL GFNGETSEGK
GAVTDLLKKR CVDEKAAVRR AALLLVTKLT SLMGGCFDGS ILKTMGTSCS DPLISIRKAA
VSAISEAFRI CTDEIVTTEW LHSVPRMIMD NETSIQEECE NVFHELVLER ILRAGNVLSP
DSASLPNNRN TTSKDLDRDI EALFPEGVLV LLRELCNSEV SPWVTKICGS LGKKKRLKPR
VALALQCIIK ESESLWLSRS MPINRWTAPA GAWFLLSEVS VYLSKSVEWE FLHHHWQLLD
KNDVQGLDEQ GDEQGVECNS STWAGDRVCL LQTISNVSLQ LPAEPAADLA DNLLKKIENF
NLHSAEVDAH VKALKTLCKK KASTSEEADM LVKKWVEQVS LKASKVTEKY IEGVSSHNHS
FVTPATLGSR RSKRLDTVSK KLSKAVTAVY TIGSCVIIYP SADTTKIVPF LHTVITSGNS
DSKLKNKLPQ ANVCLKQKAP LLYSQSWLTM AKMCLADGKL AKRYLPLFAQ ELEKSDCAAL
RNNLVVAMTD FCVHYTAMIE CYIPKITKRL RDPCEVVRRQ TFILLSRLLQ RDYVKWRGVL
FLRFLLSLVD ESEKIRRLAD FLFGSILKVK APLLAYNSFV EAIYVLNDCH AHTGHSNPDS
KQSRTKDQVF SIRGNDERAR SKRMQIYVTL LKQMAPEHLL ATFAKLCAEI LAAASDGMLN
IEDVTGQSVL QDAFQILACK EIRLSVSRGA SSETADIEEE GGDAATAKGR AITHAVRKGL
IQNTIPIFIE LKRLLESKNS PLTGSLMDCL RVLLKDYKNE IEEMLVADKQ LQKELVYDMQ
KHEAAKARSM ANQGVACGTS HRNGEPEASA ASEENVRDSG LESRVVSAAA DVVAAKAARS
VLREVNGGAA TPPLSAMSVP KLRSSRGVSQ SGRPSADVLE SLRRRPTFMS DDES
